Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Academic Article

abstract

• To identify potential Sec4 effectors, we isolated high copy suppressors of a Sec4 effector domain mutant. The most potent of these was found to be SEC9, a gene required for post-Golgi transport. The sole essential domain of Sec9 has significant sequence similarity to the neuronal protein SNAP-25, a component of the SNARE complex, that is implicated in vesicle targeting and fusion. Analogous to SNAP-25, Sec9 is bound to the yeast plasma membrane and is absent from post-Golgi vesicles. Furthermore, Sec9 is physically associated with two proteins that are homologous to components of the neuronal SNARE complex. Our results identify Sec9 as the yeast cognate of SNAP-25 and suggest that SNARE complexes acting at specific stages of vesicular transport serve as the ultimate targets of regulation by members of the Sec4/Ypt1/Rab family of GTPases.

authors

• Bankaitis, Vytas

published proceedings

• Cell

author list (cited authors)

• Brennwald, P., Kearns, B., Champion, K., Kernen, S., Bankaitis, V., & Novick, P.

citation count

• 322

complete list of authors

• Brennwald, P||Kearns, B||Champion, K||Keränen, S||Bankaitis, V||Novick, P

publication date

• January 1994

publisher

• Elsevier  Publisher

published in

• Cell  Journal

keywords

• Amino Acid Sequence
• Cell Membrane
• Exocytosis
• Fungal Proteins
• GTP-Binding Proteins
• Membrane Proteins
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Nerve Tissue Proteins
• Qa-SNARE Proteins
• Qc-SNARE Proteins
• R-SNARE Proteins
• Rab GTP-Binding Proteins
• Saccharomyces Cerevisiae
• Saccharomyces Cerevisiae Proteins
• Structure-Activity Relationship
• Synaptosomal-Associated Protein 25

Digital Object Identifier (DOI)

• 10.1016/0092-8674(94)90194-5

start page

• 245

end page

• 258

volume

• 79

issue

• 2

URL

• http://dx.doi.org/10.1016/0092-8674(94)90194-5